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New page: left|200px<br /><applet load="3bez" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bez, resolution 2.76Å" /> '''Crystal structure of...
 
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[[Image:3bez.jpg|left|200px]]<br /><applet load="3bez" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3bez, resolution 2.76&Aring;" />
'''Crystal structure of Escherichia coli Signal peptide peptidase (SppA), SeMet crystals'''<br />


==About this Structure==
==Crystal structure of Escherichia coli Signal peptide peptidase (SppA), SeMet crystals==
3BEZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEZ OCA].  
<StructureSection load='3bez' size='340' side='right'caption='[[3bez]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
[[Category: Escherichia coli]]
== Structural highlights ==
[[Category: Single protein]]
<table><tr><td colspan='2'>[[3bez]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BEZ FirstGlance]. <br>
[[Category: Paetzel, M.]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.76&#8491;</td></tr>
[[Category: bacterial]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
[[Category: hydrolase]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bez OCA], [https://pdbe.org/3bez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bez RCSB], [https://www.ebi.ac.uk/pdbsum/3bez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bez ProSAT]</span></td></tr>
[[Category: inner membrane]]
</table>
[[Category: membrane]]
== Evolutionary Conservation ==
[[Category: protease]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: transmembrane]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/be/3bez_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bez ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Signal peptide peptidase (Spp) is the enzyme responsible for cleaving the remnant signal peptides left behind in the membrane following Sec-dependent protein secretion. Spp activity appears to be present in all cell types, eukaryotic, prokaryotic and archaeal. Here we report the first structure of a signal peptide peptidase, that of the Escherichia coli SppA (SppA(EC)). SppA(EC) forms a tetrameric assembly with a novel bowl-shaped architecture. The bowl has a dramatically hydrophobic interior and contains four separate active sites that utilize a Ser/Lys catalytic dyad mechanism. Our structural analysis of SppA reveals that while in many Gram-negative bacteria as well as characterized plant variants, a tandem duplication in the protein fold creates an intact active site at the interface between the repeated domains, other species, particularly Gram-positive and archaeal organisms, encode half-size, unduplicated SppA variants that could form similar oligomers to their duplicated counterparts, but using an octamer arrangement and with the catalytic residues provided by neighboring monomers. The structure reveals a similarity in the protein fold between the domains in the periplasmic Ser/Lys protease SppA and the monomers seen in the cytoplasmic Ser/His/Asp protease ClpP. We propose that SppA may, in addition to its role in signal peptide hydrolysis, have a role in the quality assurance of periplasmic and membrane-bound proteins, similar to the role that ClpP plays for cytoplasmic proteins.


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:37:41 2008''
Crystal structure of a bacterial signal Peptide peptidase.,Kim AC, Oliver DC, Paetzel M J Mol Biol. 2008 Feb 15;376(2):352-66. Epub 2007 Dec 4. PMID:18164727<ref>PMID:18164727</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3bez" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Paetzel M]]
Retrieved from "https://proteopedia.org/3bez"